Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 337, Issue 4, Pages 1125-1132Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2005.09.162
Keywords
glutathione transferase; TEF4; EFIB gamma; elongation factor; yeast; Yarrowia lipolytica; cloning; sequence; expression; recombinant
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The TEF4 gene of the non-saccharomyces yeast Yarrowia lipolytica encodes an EF1B gamma protein with structural similarity to the glutathione transferases (GSTs). This 1203 bp gene was cloned, over-expressed in Escherichia coli, and the recombinant protein characterized. DNA sequencing of the cloned gene agreed with the recently completed Y. lipolytica genome and showed 100%) identity to a previously reported 30-residue N-terminal sequence for a 110 kDa Y lipolytica GST, except that it encoded two additional N-terminal residues (N-Met-Ser-). The recombinant protein (subunit M, 52 kDa) was found not to possess GST activity with 1-chloro-2,4-dinitrobenzene. Partial tryptic digestion released two fragments of M-r, 22 and 18 kDa, which we interpret as N- and C-terminal dornains. Homology modeling confirmed that the N-terminal domain of Y. lipoytica TEF4 encodes a GST-like protein. (c) 2005 Elsevier Inc. All rights reserved.
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